ID   A4TXK6_9PROT            Unreviewed;       341 AA.
AC   A4TXK6;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   13-SEP-2023, entry version 44.
DE   RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024,
GN   ECO:0000313|EMBL:CAM75363.1};
GN   ORFNames=MGR_2448 {ECO:0000313|EMBL:CAM75363.1};
OS   Magnetospirillum gryphiswaldense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM75363.1};
RN   [1] {ECO:0000313|EMBL:CAM75363.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MSR-1 {ECO:0000313|EMBL:CAM75363.1};
RX   PubMed=17449609; DOI=10.1128/JB.00119-07;
RA   Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA   Reinhardt R., Schueler D.;
RT   "Comparative genome analysis of four magnetotactic bacteria reveals a
RT   complex set of group-specific genes implicated in magnetosome
RT   biomineralization and function.";
RL   J. Bacteriol. 189:4899-4910(2007).
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group. {ECO:0000256|HAMAP-
CC       Rule:MF_00024}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|HAMAP-Rule:MF_00024}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_00024}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family.
CC       {ECO:0000256|ARBA:ARBA00006263, ECO:0000256|HAMAP-Rule:MF_00024}.
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DR   EMBL; CU459003; CAM75363.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TXK6; -.
DR   UniPathway; UPA00148; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00024; CobD_CbiB; 1.
DR   InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR   NCBIfam; TIGR00380; cobal_cbiB; 1.
DR   PANTHER; PTHR34308; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR   PANTHER; PTHR34308:SF1; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR   Pfam; PF03186; CobD_Cbib; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00024};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00024}.
FT   TRANSMEM        81..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        108..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        179..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        228..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        318..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   341 AA;  37369 MW;  C8A382D872750559 CRC64;
     MFHDFAMVRA MLPLFTQFGH APDGLFLLFL ALGLDAVLGE MSWLFRLIPH PVVLIGRAIA
     ALDRRLNKPE RSEAERKVRG IVMVLVLVGL SALIGAVISF VARVLPHAWV IEVFVVTTLL
     AQRGLFEHVD DVARALQHKG LEAGRYAVSR IVGRDPQSLD EHGVCRAAIE SLAENFSDAV
     VAPVFWYVLF GLPGILVYKT VNTLDSMVGY RNEKYRAFGW ASARLDDVLN LIPARLAGLI
     IALAALVAAR GNPFRAITTM IRDARHHKSP NSGWPEASMA GALGLALGGP RKYPGLVVDE
     KWIGKGRARA TFADIDRALH LFSAACLMDA GLVILVWWLQ V
//